DDB2_XENTR
ID DDB2_XENTR Reviewed; 501 AA.
AC Q66JG1;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=DNA damage-binding protein 2;
DE AltName: Full=Damage-specific DNA-binding protein 2;
GN Name=ddb2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein, which is both involved in DNA repair and protein
CC ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box)
CC complexes, respectively. Core component of the UV-DDB complex (UV-
CC damaged DNA-binding protein complex), a complex that recognizes UV-
CC induced DNA damage and recruit proteins of the nucleotide excision
CC repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB
CC complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-
CC 4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also
CC functions as the substrate recognition module for the DCX (DDB2-CUL4-X-
CC box) E3 ubiquitin-protein ligase complex DDB2-CUL4-ROC1 (also known as
CC CUL4-DDB-ROC1 and CUL4-DDB-RBX1). The DDB2-CUL4-ROC1 complex may
CC ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-
CC induced DNA damage. The ubiquitination of histones may facilitate their
CC removal from the nucleosome and promote subsequent DNA repair.
CC {ECO:0000250|UniProtKB:Q92466}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the UV-DDB complex which includes ddb1 and ddb2
CC (By similarity). Component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-
CC protein ligase complex that includes cul4a, or cul4b, ddb1, ddb2 and
CC rbx1. A large number of other DCX complexes may also exist in which an
CC alternate substrate targeting subunit replaces ddb2. These targeting
CC subunits are generally known as DCAF (ddb1- and cul4-associated factor)
CC or CDW (cul4-ddb1-associated WD40-repeat) proteins (By similarity).
CC {ECO:0000250|UniProtKB:Q92466}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92466}.
CC Chromosome {ECO:0000250|UniProtKB:Q92466}. Note=Accumulates at sites of
CC DNA damage following UV irradiation. {ECO:0000250|UniProtKB:Q92466}.
CC -!- DOMAIN: The DWD box is required for interaction with ddb1.
CC {ECO:0000250|UniProtKB:Q92466}.
CC -!- DOMAIN: Interblade loops of the WD repeat region mediate most of the
CC interaction with DNA. A hairpin between blades 5 and 6 inserts into DNA
CC minor groove and mediates recognition of lesions and separation of the
CC damaged and undamaged strands (By similarity).
CC {ECO:0000250|UniProtKB:Q92466}.
CC -!- SIMILARITY: Belongs to the WD repeat DDB2/WDR76 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC080928; AAH80928.1; -; mRNA.
DR RefSeq; NP_001008203.1; NM_001008202.1.
DR AlphaFoldDB; Q66JG1; -.
DR SMR; Q66JG1; -.
DR PaxDb; Q66JG1; -.
DR DNASU; 493565; -.
DR GeneID; 493565; -.
DR KEGG; xtr:493565; -.
DR CTD; 1643; -.
DR Xenbase; XB-GENE-971828; ddb2.
DR eggNOG; KOG4328; Eukaryota.
DR HOGENOM; CLU_036401_0_0_1; -.
DR InParanoid; Q66JG1; -.
DR OMA; DSIFGNM; -.
DR OrthoDB; 559605at2759; -.
DR PhylomeDB; Q66JG1; -.
DR TreeFam; TF331587; -.
DR Reactome; R-XTR-5689880; Ub-specific processing proteases.
DR Reactome; R-XTR-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-XTR-5696400; Dual Incision in GG-NER.
DR Reactome; R-XTR-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000003980; Expressed in brain and 12 other tissues.
DR ExpressionAtlas; Q66JG1; baseline.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0009411; P:response to UV; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR033312; DDB2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15169; PTHR15169; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Chromosome; DNA damage; DNA repair; DNA-binding; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..501
FT /note="DNA damage-binding protein 2"
FT /id="PRO_0000351091"
FT REPEAT 126..160
FT /note="WD 1"
FT REPEAT 168..203
FT /note="WD 2"
FT REPEAT 212..247
FT /note="WD 3"
FT REPEAT 253..296
FT /note="WD 4"
FT REPEAT 299..339
FT /note="WD 5"
FT REPEAT 353..396
FT /note="WD 6"
FT REPEAT 406..430
FT /note="WD 7"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..346
FT /note="Photolesion recognition"
FT /evidence="ECO:0000250|UniProtKB:Q92466"
FT REGION 452..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 265..283
FT /note="DWD box"
FT COMPBIAS 24..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 56609 MW; 37FC8268CC0CE057 CRC64;
MPPKRATRGR RNVELSSEEE EEQEEVSPGK RKRDIEKNGE ARLKKPSKKR SGQQCASDVP
CSSKESDCGT NLTNKGDKQR SIVHYLYRST LGGNVRAKYL QTPFLRSLAS YILYRTNSPF
DRRVTTLEWH PTHPNTVAVG SKGGDIILWD YEELNNTLIP GIGAGGCITG MKFDPFNPNQ
LYTSSVAGST VLQDFSGRNI QTFTNTEDWA MWYCSLDVSA ERQCVVTGDN VGNVVLLETC
GKEIWKLRLH KKKVTHVEFN PRCDWLLASA SVDQTVKLWD LRNIKDKSSY LYTLPHARGV
NSAYFSPWDG AKLLTTDQHS EIRVYSACDW AKPQHIIPHP HRQFQHLTAI KATWHPRYDL
IVVGRYPDPL FPGYMSDELR TVDVFDGQKG NIVCQLYDPY ASGIVSLNKF NPMGDLLASG
MGFNILIWSR EILLMMKQEE MMKALREKGV SVGRKELPNS RLPHSSAPRE KPGNKGSTTE
SSKTRTVRES SKRGKHKDPG K
